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BTK (Bruton agammaglobulinemia tyrosine kinase)

Identity

Other namesAGMX1
AT
ATK
BPK
IMD1
MGC126261
MGC126262
PSCTK1
XLA
HGNC (Hugo) BTK
LocusID (NCBI) 695
Location Xq22.1
Location_base_pair Starts at 100604435 and ends at 100641212 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Note BTK (Bruton's tyrosine kinase) is a cytoplasmic non-receptor protein tyrosine kinase that is essential for B cell maturation in humans and mice.

DNA/RNA

Description The gene spans over 36 kb and is composed of 19 exons, both in human and mouse.
Transcription The transcript is about 2,573 bps in human and about 2,477 bps mice and has UTR regions in exons 1, 2 and 19.

Protein

 
  Table 1: BTK dependent receptor signaling cascades.
Description The BTK protein is a 77 kDa protein of 659 amino acids. Translation of the BTK transcript starts at the ATG site that is located in exon 2 and ends in exon 19.
The BTK protein is composed of an N-terminal Pleckstrin homology (PH) domain followed three protein interacting domains: Tec homology (TH) region, Src homology 3 (SH3) domain and SH2 domain. A tyrosine-kinase catalytic domain is located at the C-terminal end. Two tyrosine phosphorylation sites are located at the positions Y223 and Y551, which are located in the SH3 and kinase domain, respectively. Both phosphorylation sites play a pivotal role in the activation of BTK. Y551 is transphosphorylated by Syk (or Lyn) kinases which promotes the catalytic activity of BTK, with subsequent autophosphorylation at position Y223.
Expression BTK is expressed in all cell lineages of the hematopoietic system, except for T cells. Therefore BTK expression is found in B lymphocytes, platelets, erythroid and myeloid cells (monocytes, macrophages, granulocytes and dendritic cells). Within the B cell lineage, BTK is already expressed in the earliest detectable B cell precursors, and expression is downregulated in plasma cells.
Localisation The protein is predominantly localized in the cytoplasm. BTK activation upon receptor signaling results in translocation of BTK protein from the cytoplasm to the membrane. The membrane association of BTK is dependent on the interaction of its PH domain with PIP3 (phosphatidylinositol (3,4,5)-trisphosphate), which is a second messenger that is synthesized from PIP2 by PI3K (phosphoinositide-3 kinase). The translocation to the membrane brings the BTK protein in close proximity to the Lyn en Syk kinases that transphosphorylate BTK at tyrosine Y551. The E41K gain-of-function BTK mutant, in which the E41 residue is mutated in to a lysine residue, manifests increased membrane localization in quiescent cells, independent of PI3K activity, probably resulting from increased affinity for PIP2. Transforming activity is kinase-domain dependent and is potentiated by introduction of a second mutation at position Y223.
Function BTK is a signaling mediator downstream of a variety of receptors in several different cell types (listed in Table 1), including the B cell receptor (BCR).
Homology BTK belongs to the TEC family of cytoplasmic tyrosine kinases. This family is composed of TEC, BTK, TXK/RLK, ITK/EMT, and BMX. Btk is highly conserved between mouse and human.

Implicated in

Entity Pre-B cell tumors
Note Truncated BTK forms in human BCR-ABL1 + leukemia
BTK is constitutively phosphorylated by the oncogenic BCR- ABL1 fusion product. Inhibition of BTK activity specifically induces apoptosis in BCR-ABL1+ leukemia cells to a similar extent as inhibition of BCR-ABL1 kinase activity itself. BCR-ABL1 cannot directly bind to full-length BTK, but induces the expression of a truncated BTK splice variant that acts as a linker between the two kinases. Thus, truncated BTK enables BCR-ABL1-dependent activation of full-length BTK, which initiates downstream survival signals and mimics pre-B cell receptor signaling.
Defective expression of BTK in acute lymphoblastic leukemia (ALL)
In an analysis of BTK protein and mRNA expression in infant B-lineage leukemia cells variable but often reduced levels of BTK expression was found. RT-PCR revealed the presence of aberrant transcripts which would encode BTK proteins with either a deleted or a truncated kinase domain. In infant pre-B MLL-AF4+ leukemia cells full-length BTK was detectable in only half of the cases, whereas in ALL cells harboring other fusion genes (including BCR-ABL1, E2A- PBX1 and TEL- AML1) full-length BTK was typically co-expressed with kinase-deficient variants. Thus, lack of BTK or expression of dominant-negative BTK splice variants in B cell precursor leukemia cells can inhibit differentiation beyond the pre-B cell stage and protect from radiation-induced apoptosis.
Btk as a tumor suppressor in pre-B cell leukemia in mice
Expression of the pre-B cell receptor (pre-BCR) leads to activation of the adaptor molecule Slp65 (also termed Bash or Blnk) and Btk. Spontaneous pre-B cell leukemia development in Slp65-deficient mice demonstrate that Slp65 acts as a tumor suppressor. Slp65 and Btk have a synergistic role in the developmental progression of large cycling into small resting pre-B cells. Btk/Slp65 double mutant mice have a dramatically increased pre-B cell tumor incidence (approximately 75%, 16 wk of age), as compared with Slp65 single deficient mice (<10%). Therefore, Btk cooperates with Slp65 as a tumor suppressor in pre-B cells. Moreover, transgenic expression of a constitutive active form of Btk, the E41K-Y223F mutant, prevented tumor formation in Btk/Slp65 double mutant mice, indicating that constitutive active Btk can substitute for Slp65 as a tumor suppressor. Using a kinase-inactive K430R-Btk mutant, it was shown that Btk exerts its tumor suppressor function in pre-B cells as an adaptor protein, independent of its catalytic activity. Furthermore, loss of Btk and Tec increases the tumor frequency in Eµ-myc transgenic mice, expressing the c-myc oncogenic transcription factor that promotes both proliferation and differentiation.
  
Entity X-linked agammaglobulinemia (XLA).
Note In 1993 BTK was identified as the gene defective in the human immunodeficiency disease X-linked agammaglobulinemia (XLA). The XLA disease, which was first described by Dr. O.C. Bruton in 1952, is characterized by protracted and recurrent bacterial infections.
Clinical manifestations of XLA
XLA Patients have less than 1% of the normal number of peripheral B cells. Serum levels of all Ig classes are very low due to the lack of plasma cells in the secondary lymphoid organs. In XLA patients, B cell development is almost completely arrested at the pre-B cell stage: the pre-B cell fraction mainly consists of small cells, suggesting that Btk is necessary for their proliferative expansion. Heterozygous female XLA carriers do not have clinical or immunological symptoms, but manifest a unilateral X chromosome inactivation in the peripheral blood B lymphocyte population, because of a selective disadvantage of cells that have the defective Btk gene on the active X chromosome. In contrast to XLA, Btk-deficiency in the mouse, termed X-linked immunodeficiency (xid), is associated with a very mild early B cell developmental block, but with impaired maturation and poor survival of peripheral B cells. XLA is a heterogeneous disease, even within single families and no correlation has been observed between the position of the mutation and phenotypic variables, such as age at time of diagnosis or severity of the clinical or immunological symptoms. Therefore, this heterogeneity might be related to other genetic or environmental factors.
Mutations in BTK gene that cause XLA
The BTK mutations that have been identified in XLA patients compromise BTK function either through gross structural changes (such as deletions or altered protein folding) or through specific loss of functionally relevant residues. Strikingly, none of the found unique missense mutations found in XLA patients is located in the SH3 domain of BTK, which harbors the Y223 tyrosine residue. An international registry for XLA (http://bioinf.uta.fi/BTKbase/) shows that mutations in all domains of the BTK gene cause the disease.
Approximately 80-90% of the patients that have agammaglobulinemia patients have a deficiency of the BTK protein. The other about 15% of the agammaglobulinemia cases are caused by defects in autosomal genes such as the constant region of immunoglobulin (Ig) heavy chain, λ5, (IGLL), Igα (CD79a), Igβ (CD79b), or SLP65 (BLNK) resemble the clinical manifestation of XLA.
  

External links

Nomenclature
HGNC (Hugo)BTK   1133
Cards
AtlasBTKID851chXq22
Entrez_Gene (NCBI)BTK  695  Bruton agammaglobulinemia tyrosine kinase
GeneCards (Weizmann)BTK
Ensembl (Hinxton)ENSG00000010671 [Gene_View]  chrX:100604435-100641212 [Contig_View]  BTK [Vega]
ICGC DataPortalENSG00000010671
cBioPortalBTK
AceView (NCBI)BTK
Genatlas (Paris)BTK
WikiGenes695
SOURCE (Princeton)NM_000061 NM_001287344 NM_001287345
Genomic and cartography
GoldenPath (UCSC)BTK  -  Xq22.1   chrX:100604435-100641212 -  Xq21.33-q22   [Description]    (hg19-Feb_2009)
EnsemblBTK - Xq21.33-q22 [CytoView]
Mapping of homologs : NCBIBTK [Mapview]
OMIM300300   300755   307200   
Gene and transcription
Genbank (Entrez)AF153364 AF153755 AF153756 AF153757 AF153758
RefSeq transcript (Entrez)NM_000061 NM_001287344 NM_001287345
RefSeq genomic (Entrez)AC_000155 NC_000023 NC_018934 NG_009616 NT_011651 NW_001842387 NW_004929444
Consensus coding sequences : CCDS (NCBI)BTK
Cluster EST : UnigeneHs.733206 [ NCBI ]
CGAP (NCI)Hs.733206
Alternative Splicing : Fast-db (Paris)GSHG0032229
Alternative Splicing GalleryENSG00000010671
Gene ExpressionBTK [ NCBI-GEO ]     BTK [ SEEK ]   BTK [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ06187 (Uniprot)
NextProtQ06187  [Medical]
With graphics : InterProQ06187
Splice isoforms : SwissVarQ06187 (Swissvar)
Catalytic activity : Enzyme2.7.10.2 [ Enzyme-Expasy ]   2.7.10.22.7.10.2 [ IntEnz-EBI ]   2.7.10.2 [ BRENDA ]   2.7.10.2 [ KEGG ]   
Domaine pattern : Prosite (Expaxy)PH_DOMAIN (PS50003)    PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_TYR (PS00109)    SH2 (PS50001)    SH3 (PS50002)    ZF_BTK (PS51113)   
Domains : Interpro (EBI)Kinase-like_dom [organisation]   PH_like_dom [organisation]   Pleckstrin_homology [organisation]   Prot_kinase_dom [organisation]   Protein_kinase_ATP_BS [organisation]   Ser-Thr/Tyr_kinase_cat_dom [organisation]   SH2 [organisation]   SH3_domain [organisation]   Tyr_kinase_AS [organisation]   Tyr_kinase_cat_dom [organisation]   Znf_Btk_motif [organisation]  
Related proteins : CluSTrQ06187
Domain families : Pfam (Sanger)BTK (PF00779)    PH (PF00169)    Pkinase_Tyr (PF07714)    SH2 (PF00017)    SH3_1 (PF00018)   
Domain families : Pfam (NCBI)pfam00779    pfam00169    pfam07714    pfam00017    pfam00018   
Domain families : Smart (EMBL)BTK (SM00107)  PH (SM00233)  SH2 (SM00252)  SH3 (SM00326)  TyrKc (SM00219)  
DMDM Disease mutations695
Blocks (Seattle)Q06187
PDB (SRS)1AWW    1AWX    1B55    1BTK    1BWN    1K2P    1QLY    2GE9    2Z0P    3GEN    3K54    3OCS    3OCT    3P08    3PIX    3PIY    3PIZ    3PJ1    3PJ2    3PJ3    4NWM   
PDB (PDBSum)1AWW    1AWX    1B55    1BTK    1BWN    1K2P    1QLY    2GE9    2Z0P    3GEN    3K54    3OCS    3OCT    3P08    3PIX    3PIY    3PIZ    3PJ1    3PJ2    3PJ3    4NWM   
PDB (IMB)1AWW    1AWX    1B55    1BTK    1BWN    1K2P    1QLY    2GE9    2Z0P    3GEN    3K54    3OCS    3OCT    3P08    3PIX    3PIY    3PIZ    3PJ1    3PJ2    3PJ3    4NWM   
PDB (RSDB)1AWW    1AWX    1B55    1BTK    1BWN    1K2P    1QLY    2GE9    2Z0P    3GEN    3K54    3OCS    3OCT    3P08    3PIX    3PIY    3PIZ    3PJ1    3PJ2    3PJ3    4NWM   
Human Protein AtlasENSG00000010671 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasQ06187
HPRD02248
IPIIPI00029132   IPI00816615   IPI00746467   IPI00815757   IPI00816083   IPI00654849   IPI01009200   IPI00854612   IPI00973083   IPI01018631   IPI00844337   IPI00646149   
Protein Interaction databases
DIP (DOE-UCLA)Q06187
IntAct (EBI)Q06187
FunCoupENSG00000010671
BioGRIDBTK
InParanoidQ06187
Interologous Interaction database Q06187
IntegromeDBBTK
STRING (EMBL)BTK
Ontologies - Pathways
Ontology : AmiGOresponse to reactive oxygen species  toll-like receptor signaling pathway  adaptive immune response  histamine secretion by mast cell  regulation of B cell cytokine production  MyD88-dependent toll-like receptor signaling pathway  regulation of B cell apoptotic process  protein tyrosine kinase activity  protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  protein binding  ATP binding  phosphatidylinositol-3,4,5-trisphosphate binding  nucleus  cytoplasm  cytosol  cytosol  plasma membrane  plasma membrane  transcription, DNA-templated  protein phosphorylation  I-kappaB kinase/NF-kappaB signaling  mesoderm development  response to organic substance  peptidyl-tyrosine phosphorylation  calcium-mediated signaling  cytoplasmic vesicle  toll-like receptor 2 signaling pathway  toll-like receptor 4 signaling pathway  intracellular signal transduction  Fc-epsilon receptor signaling pathway  toll-like receptor TLR1:TLR2 signaling pathway  toll-like receptor TLR6:TLR2 signaling pathway  B cell activation  mast cell granule  identical protein binding  intracellular membrane-bounded organelle  innate immune response  membrane raft  positive regulation of B cell differentiation  protein autophosphorylation  metal ion binding  cell maturation  perinuclear region of cytoplasm  B cell receptor signaling pathway  positive regulation of NF-kappaB transcription factor activity  apoptotic signaling pathway  
Ontology : EGO-EBIresponse to reactive oxygen species  toll-like receptor signaling pathway  adaptive immune response  histamine secretion by mast cell  regulation of B cell cytokine production  MyD88-dependent toll-like receptor signaling pathway  regulation of B cell apoptotic process  protein tyrosine kinase activity  protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  protein binding  ATP binding  phosphatidylinositol-3,4,5-trisphosphate binding  nucleus  cytoplasm  cytosol  cytosol  plasma membrane  plasma membrane  transcription, DNA-templated  protein phosphorylation  I-kappaB kinase/NF-kappaB signaling  mesoderm development  response to organic substance  peptidyl-tyrosine phosphorylation  calcium-mediated signaling  cytoplasmic vesicle  toll-like receptor 2 signaling pathway  toll-like receptor 4 signaling pathway  intracellular signal transduction  Fc-epsilon receptor signaling pathway  toll-like receptor TLR1:TLR2 signaling pathway  toll-like receptor TLR6:TLR2 signaling pathway  B cell activation  mast cell granule  identical protein binding  intracellular membrane-bounded organelle  innate immune response  membrane raft  positive regulation of B cell differentiation  protein autophosphorylation  metal ion binding  cell maturation  perinuclear region of cytoplasm  B cell receptor signaling pathway  positive regulation of NF-kappaB transcription factor activity  apoptotic signaling pathway  
Pathways : BIOCARTABCR Signaling Pathway [Genes]    Phosphoinositides and their downstream targets. [Genes]    Fc Epsilon Receptor I Signaling in Mast Cells [Genes]   
Pathways : KEGGNF-kappa B signaling pathway    Osteoclast differentiation    B cell receptor signaling pathway    Fc epsilon RI signaling pathway    Primary immunodeficiency   
Protein Interaction DatabaseBTK
Wikipedia pathwaysBTK
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)BTK
snp3D : Map Gene to Disease695
SNP (GeneSNP Utah)BTK
SNP : HGBaseBTK
Genetic variants : HAPMAPBTK
Exome VariantBTK
1000_GenomesBTK 
ICGC programENSG00000010671 
Somatic Mutations in Cancer : COSMICBTK 
CONAN: Copy Number AnalysisBTK 
Mutations and Diseases : HGMDBTK
Mutations and Diseases : intOGenBTK
Genomic VariantsBTK  BTK [DGVbeta]
dbVarBTK
ClinVarBTK
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM300300    300755    307200   
MedgenBTK
GENETestsBTK
Disease Genetic AssociationBTK
Huge Navigator BTK [HugePedia]  BTK [HugeCancerGEM]
General knowledge
Homologs : HomoloGeneBTK
Homology/Alignments : Family Browser (UCSC)BTK
Phylogenetic Trees/Animal Genes : TreeFamBTK
Chemical/Protein Interactions : CTD695
Chemical/Pharm GKB GenePA25454
Clinical trialBTK
Cancer Resource (Charite)ENSG00000010671
Other databases
Other databasehttp://bioinf.uta.fi/BTKbase/
Probes
Litterature
PubMed226 Pubmed reference(s) in Entrez
CoreMineBTK
iHOPBTK
OncoSearchBTK

Bibliography

Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia.
Tsukada S, Saffran DC, Rawlings DJ, Parolini O, Allen RC, Klisak I, Sparkes RS, Kubagawa H, Mohandas T, Quan S, et al.
Cell. 1993 Jan 29;72(2):279-90.
PMID 8425221
 
The gene involved in X-linked agammaglobulinaemia is a member of the src family of protein-tyrosine kinases.
Vetrie D, Vorechovsky I, Sideras P, Holland J, Davies A, Flinter F, Hammarstrom L, Kinnon C, Levinsky R, Bobrow M, et al.
Nature. 1993 Jan 21;361(6409):226-33.
PMID 8380905
 
Defective B cell development and function in Btk-deficient mice.
Khan WN, Alt FW, Gerstein RM, Malynn BA, Larsson I, Rathbun G, Davidson L, Muller S, Kantor AB, Herzenberg LA, et al.
Immunity. 1995 Sep;3(3):283-99.
PMID 7552994
 
Activation of Bruton's tyrosine kinase (BTK) by a point mutation in its pleckstrin homology (PH) domain.
Li T, Tsukada S, Satterthwaite A, Havlik MH, Park H, Takatsu K, Witte ON.
Immunity. 1995 May;2(5):451-60.
PMID 7538439
 
Inactivation of Btk by insertion of lacZ reveals defects in B cell development only past the pre-B cell stage.
Hendriks RW, de Bruijn MF, Maas A, Dingjan GM, Karis A, Grosveld F.
EMBO J. 1996 Sep 16;15(18):4862-72.
PMID 8890160
 
Regulation of Btk function by a major autophosphorylation site within the SH3 domain.
Park H, Wahl MI, Afar DE, Turck CW, Rawlings DJ, Tam C, Scharenberg AM, Kinet JP, Witte ON.
Immunity. 1996 May;4(5):515-25.
PMID 8630736
 
BTK as a mediator of radiation-induced apoptosis in DT-40 lymphoma B cells.
Uckun FM, Waddick KG, Mahajan S, Jun X, Takata M, Bolen J, Kurosaki T.
Science. 1996 Aug 23;273(5278):1096-100.
PMID 8688094
 
Rational design and synthesis of a novel anti-leukemic agent targeting Bruton's tyrosine kinase (BTK), LFM-A13 [alpha-cyano-beta-hydroxy-beta-methyl-N-(2, 5-dibromophenyl)propenamide].
Mahajan S, Ghosh S, Sudbeck EA, Zheng Y, Downs S, Hupke M, Uckun FM.
J Biol Chem. 1999 Apr 2;274(14):9587-99.
PMID 10092645
 
Genetic defect in human X-linked agammaglobulinemia impedes a maturational evolution of pro-B cells into a later stage of pre-B cells in the B-cell differentiation pathway.
Nomura K, Kanegane H, Karasuyama H, Tsukada S, Agematsu K, Murakami G, Sakazume S, Sako M, Tanaka R, Kuniya Y, Komeno T, Ishihara S, Hayashi K, Kishimoto T, Miyawaki T.
Blood. 2000 Jul 15;96(2):610-7.
PMID 10887125
 
Impaired precursor B cell differentiation in Bruton's tyrosine kinase-deficient mice.
Middendorp S, Dingjan GM, Hendriks RW.
J Immunol. 2002 Mar 15;168(6):2695-703.
PMID 11884435
 
Defective expression of Bruton's tyrosine kinase in acute lymphoblastic leukemia.
Goodman PA, Wood CM, Vassilev AO, Mao C, Uckun FM.
Leuk Lymphoma. 2003 Jun;44(6):1011-8.
PMID 12854903
 
Bruton's tyrosine kinase cooperates with the B cell linker protein SLP-65 as a tumor suppressor in Pre-B cells.
Kersseboom R, Middendorp S, Dingjan GM, Dahlenborg K, Reth M, Jumaa H, Hendriks RW.
J Exp Med. 2003 Jul 7;198(1):91-8.
PMID 12835482
 
The pre-BCR checkpoint as a cell-autonomous proliferation switch.
Hendriks RW, Middendorp S.
Trends Immunol. 2004 May;25(5):249-56.
PMID 15099565
 
Mimicry of a constitutively active pre-B cell receptor in acute lymphoblastic leukemia cells.
Feldhahn N, Klein F, Mooster JL, Hadweh P, Sprangers M, Wartenberg M, Bekhite MM, Hofmann WK, Herzog S, Jumaa H, Rowley JD, Muschen M.
J Exp Med. 2005 Jun 6;201(11):1837-52.
PMID 15939795
 
Deficiency of Bruton's tyrosine kinase in B cell precursor leukemia cells.
Feldhahn N, Río P, Soh BN, Liedtke S, Sprangers M, Klein F, Wernet P, Jumaa H, Hofmann WK, Hanenberg H, Rowley JD, Müschen M.
Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13266-71.
PMID 16141323
 
B cell signaling and tumorigenesis.
Jumaa H, Hendriks RW, Reth M.
Annu Rev Immunol. 2005;23:415-45.
PMID 15771577
 
Tumor suppressor function of Bruton tyrosine kinase is independent of its catalytic activity.
Middendorp S, Zijlstra AJ, Kersseboom R, Dingjan GM, Jumaa H, Hendriks RW.
Blood. 2005 Jan 1;105(1):259-65.
PMID 15331445
 
Involvement of SLP-65 and Btk in tumor suppression and malignant transformation of pre-B cells.
Hendriks RW, Kersseboom R.
Semin Immunol. 2006 Feb;18(1):67-76.
PMID 16300960
 
BTKbase: the mutation database for X-linked agammaglobulinemia.
Valiaho J, Smith CI, Vihinen M.
Hum Mutat. 2006 Dec;27(12):1209-17.
PMID 16969761
 
Myc stimulates B lymphocyte differentiation and amplifies calcium signaling.
Habib T, Park H, Tsang M, de Alboran IM, Nicks A, Wilson L, Knoepfler PS, Andrews S, Rawlings DJ, Eisenman RN, Iritani BM.
J Cell Biol. 2007 Nov 19;179(4):717-31.
PMID 17998397
 
The Btk tyrosine kinase is a major target of the Bcr-Abl inhibitor dasatinib.
Hantschel O, Rix U, Schmidt U, Bürckstummer T, Kneidinger M, Schutze G, Colinge J, Bennett KL, Ellmeier W, Valent P, Superti-Furga G
Proc Natl Acad Sci U S A. 2007 Aug 14;104(33):13283-8.
PMID 17684099
 
Bruton's tyrosine kinase prevents activation of the anti-apoptotic transcription factor STAT3 and promotes apoptosis in neoplastic B-cells and B-cell precursors exposed to oxidative stress.
Uckun F, Ozer Z, Vassilev A.
Br J Haematol. 2007 Feb;136(4):574-89.
PMID 17367410
 
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Contributor(s)

Written03-2008Rudi W Hendriks, Pieter Fokko van Loo
Department of Pulmonary Medicine, Room Ee2251a, Erasmus MC Rotterdam, PO Box 2040 NL 3000 CA Rotterdam, The Netherlands

Citation

This paper should be referenced as such :
Hendriks, RW ; van, Loo PF
BTK (Bruton agammaglobulinemia tyrosine kinase)
Atlas Genet Cytogenet Oncol Haematol. 2009;12(1):1-4.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/BTKID851chXq22.html

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